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Q9XBN7 (BLAB4_ELIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbapenem-hydrolyzing beta-lactamase BlaB-4

Short name=CHbetaL-4
EC=3.5.2.6
Alternative name(s):
Class B carbapenemase BlaB-4
Metallo lactamase BlaB-3
Gene names
Name:blaB4
Synonyms:blaB, blaB3
OrganismElizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Taxonomic identifier238 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate By similarity.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 249227Carbapenem-hydrolyzing beta-lactamase BlaB-4
PRO_0000016952

Sites

Metal binding981Zinc 1 By similarity
Metal binding1001Zinc 1 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1611Zinc 1 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2221Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9XBN7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F5327FD6516153B5

FASTA24928,225
        10         20         30         40         50         60 
MMKKMKWALV LALGLTGLNA FGQETPEVKI EKLKDNLYVY TTYNTFNGTK YAANAVYLVT 

        70         80         90        100        110        120 
SKGVVVIDSP WGEEKFKNFT DEIYKRHGKK VIMNIATHSH DDRAGGLEYF KSLGAKTYST 

       130        140        150        160        170        180 
KMTDSILAKD NKPRAQYTFD NNKSFKVGKD EFQVYYPGKG HTADHVVVWF PKDKVLVGGC 

       190        200        210        220        230        240 
IIKSGDSKDL GFLGEAYVND WTQSVHNIQK KFPNVQYVVA GHDDWKDQTA IQHTLDLISE 


YQQKQKASN 

« Hide

References

[1]"Carbapenemases of chryseobacterium (Flavobacterium) meningosepticum: distribution of blaB and characterization of a novel metallo-beta-lactamase gene, blaB3, in the type strain, NCTC 10016."
Woodford N., Palepou M.-F.I., Babini G.S., Holmes B., Livermore D.M.
Antimicrob. Agents Chemother. 44:1448-1452(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13253 / CIP 60.57 / DSM 2800 / LMG 12279 / NBRC 12535 / NCTC 10016.
[2]"Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum."
Bellais S., Aubert D., Naas T., Nordmann P.
Antimicrob. Agents Chemother. 44:1878-1886(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13253 / CIP 60.57 / DSM 2800 / LMG 12279 / NBRC 12535 / NCTC 10016.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF162284 Genomic DNA. Translation: AAD43582.1.

3D structure databases

ProteinModelPortalQ9XBN7.
SMRQ9XBN7. Positions 27-245.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.60.15.10. 1 hit.
InterProIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view]
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMSSF56281. SSF56281. 1 hit.
PROSITEPS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLAB4_ELIME
AccessionPrimary (citable) accession number: Q9XBN7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families